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-Structure paper
| Title | Three-dimensional structure of the bacteriophage P22 tail machine. |
|---|---|
| Journal, issue, pages | EMBO J, Vol. 24, Issue 12, Page 2087-2095, Year 2005 |
| Publish date | Jun 15, 2005 |
Authors | Liang Tang / William R Marion / Gino Cingolani / Peter E Prevelige / John E Johnson / ![]() |
| PubMed Abstract | The tail of the bacteriophage P22 is composed of multiple protein components and integrates various biological functions that are crucial to the assembly and infection of the phage. The three- ...The tail of the bacteriophage P22 is composed of multiple protein components and integrates various biological functions that are crucial to the assembly and infection of the phage. The three-dimensional structure of the P22 tail machine determined by electron cryo-microscopy and image reconstruction reveals how the five types of polypeptides present as 51 subunits are organized into this molecular machine through twelve-, six- and three-fold symmetry, and provides insights into molecular events during host cell attachment and phage DNA translocation. |
External links | EMBO J / PubMed:15933718 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 23.0 Å |
| Structure data | ![]() EMDB-1119: |
| Source |
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Enterobacteria phage P22 (virus)